Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3SEQ

Crystal structure of C176A mutant of glutamine-dependent NAD+ synthetase from M. tuberculosis in complex with AMPCPP and NaAD+

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003952	molecular_function	NAD+ synthase (glutamine-hydrolyzing) activity
A	0004359	molecular_function	glutaminase activity
A	0005524	molecular_function	ATP binding
A	0005737	cellular_component	cytoplasm
A	0005886	cellular_component	plasma membrane
A	0006807	biological_process	obsolete nitrogen compound metabolic process
A	0008795	molecular_function	NAD+ synthase activity
A	0009274	cellular_component	peptidoglycan-based cell wall
A	0009435	biological_process	NAD biosynthetic process
A	0016874	molecular_function	ligase activity
A	0042802	molecular_function	identical protein binding
B	0003952	molecular_function	NAD+ synthase (glutamine-hydrolyzing) activity
B	0004359	molecular_function	glutaminase activity
B	0005524	molecular_function	ATP binding
B	0005737	cellular_component	cytoplasm
B	0005886	cellular_component	plasma membrane
B	0006807	biological_process	obsolete nitrogen compound metabolic process
B	0008795	molecular_function	NAD+ synthase activity
B	0009274	cellular_component	peptidoglycan-based cell wall
B	0009435	biological_process	NAD biosynthetic process
B	0016874	molecular_function	ligase activity
B	0042802	molecular_function	identical protein binding
C	0003952	molecular_function	NAD+ synthase (glutamine-hydrolyzing) activity
C	0004359	molecular_function	glutaminase activity
C	0005524	molecular_function	ATP binding
C	0005737	cellular_component	cytoplasm
C	0005886	cellular_component	plasma membrane
C	0006807	biological_process	obsolete nitrogen compound metabolic process
C	0008795	molecular_function	NAD+ synthase activity
C	0009274	cellular_component	peptidoglycan-based cell wall
C	0009435	biological_process	NAD biosynthetic process
C	0016874	molecular_function	ligase activity
C	0042802	molecular_function	identical protein binding
D	0003952	molecular_function	NAD+ synthase (glutamine-hydrolyzing) activity
D	0004359	molecular_function	glutaminase activity
D	0005524	molecular_function	ATP binding
D	0005737	cellular_component	cytoplasm
D	0005886	cellular_component	plasma membrane
D	0006807	biological_process	obsolete nitrogen compound metabolic process
D	0008795	molecular_function	NAD+ synthase activity
D	0009274	cellular_component	peptidoglycan-based cell wall
D	0009435	biological_process	NAD biosynthetic process
D	0016874	molecular_function	ligase activity
D	0042802	molecular_function	identical protein binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	12
Details	BINDING SITE FOR RESIDUE APC A 680

Chain	Residue
A	GLY366
A	ARG462
A	THR480
A	DND681
A	VAL367
A	SER368
A	GLY370
A	LEU371
A	ASP372
A	SER373
A	PHE397
A	LEU399

site_id	AC2
Number of Residues	21
Details	BINDING SITE FOR RESIDUE NXX A 681

Chain	Residue
A	VAL452
A	ASN456
A	GLU485
A	TRP490
A	SER491
A	THR492
A	TYR493
A	ASP497
A	PHE631
A	PHE634
A	LYS635
A	SER661
A	APC680
A	HOH736
A	HOH768
D	ARG354
D	LEU358
D	ASN471
D	GLY475
D	ILE476
D	HIS501

site_id	AC3
Number of Residues	12
Details	BINDING SITE FOR RESIDUE APC B 680

Chain	Residue
B	GLY366
B	VAL367
B	SER368
B	GLY370
B	LEU371
B	ASP372
B	SER373
B	PHE397
B	LEU399
B	ARG462
B	THR480
B	DND681

site_id	AC4
Number of Residues	18
Details	BINDING SITE FOR RESIDUE NXX B 681

Chain	Residue
B	ASN456
B	GLU485
B	TRP490
B	SER491
B	THR492
B	TYR493
B	ASP497
B	PHE631
B	PHE634
B	LYS635
B	SER661
B	APC680
B	HOH756
C	ARG354
C	LEU358
C	ASN471
C	GLY475
C	HIS501

site_id	AC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL B 682

Chain	Residue
B	TYR58
B	SER59
B	ILE60
B	GLU61
B	TYR131
B	GLN135

site_id	AC6
Number of Residues	13
Details	BINDING SITE FOR RESIDUE APC C 680

Chain	Residue
C	GLY366
C	VAL367
C	SER368
C	GLY370
C	LEU371
C	ASP372
C	SER373
C	PHE397
C	ALA398
C	LEU399
C	ARG462
C	THR480
C	DND681

site_id	AC7
Number of Residues	19
Details	BINDING SITE FOR RESIDUE NXX C 681

Chain	Residue
C	APC680
C	HOH840
B	ARG354
B	LEU358
B	ASN471
B	GLY475
B	ILE476
B	HIS501
C	ASN456
C	GLU485
C	TRP490
C	SER491
C	THR492
C	TYR493
C	ASP497
C	PHE631
C	PHE634
C	LYS635
C	SER661

site_id	AC8
Number of Residues	13
Details	BINDING SITE FOR RESIDUE APC D 680

Chain	Residue
D	GLY366
D	VAL367
D	SER368
D	GLY370
D	LEU371
D	ASP372
D	SER373
D	PHE397
D	ALA398
D	LEU399
D	ARG462
D	THR480
D	DND681

site_id	AC9
Number of Residues	17
Details	BINDING SITE FOR RESIDUE NXX D 681

Chain	Residue
A	ARG354
A	LEU358
A	ASN471
A	GLY475
A	ILE476
A	HIS501
D	TRP490
D	SER491
D	THR492
D	TYR493
D	ASP497
D	PHE631
D	PHE634
D	LYS635
D	SER661
D	APC680
D	HOH755

site_id	BC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE GOL D 682

Chain	Residue
D	ARG218
D	ALA255
D	LEU256

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	ACT_SITE: Proton acceptor; for glutaminase activity => ECO:0000255\|HAMAP-Rule:MF_02090, ECO:0000305\|PubMed:15748981, ECO:0000305\|PubMed:19270703

Chain	Residue	Details
A	GLU52
B	GLU52
C	GLU52
D	GLU52

site_id	SWS_FT_FI2
Number of Residues	4
Details	ACT_SITE: For glutaminase activity => ECO:0000255\|HAMAP-Rule:MF_02090, ECO:0000305\|PubMed:15748981, ECO:0000305\|PubMed:19270703

Chain	Residue	Details
A	LYS121
B	LYS121
C	LYS121
D	LYS121

site_id	SWS_FT_FI3
Number of Residues	4
Details	ACT_SITE: Nucleophile; for glutaminase activity => ECO:0000255\|HAMAP-Rule:MF_02090, ECO:0000305\|PubMed:15748981, ECO:0000305\|PubMed:19270703

Chain	Residue	Details
A	ALA176
B	ALA176
C	ALA176
D	ALA176

site_id	SWS_FT_FI4
Number of Residues	12
Details	BINDING: BINDING => ECO:0000255\|HAMAP-Rule:MF_02090, ECO:0007744\|PDB:3SYT

Chain	Residue	Details
A	TYR127
D	TYR127
D	SER203
D	ARG209
A	SER203
A	ARG209
B	TYR127
B	SER203
B	ARG209
C	TYR127
C	SER203
C	ARG209

site_id	SWS_FT_FI5
Number of Residues	16
Details	BINDING: BINDING => ECO:0007744\|PDB:3DLA, ECO:0007744\|PDB:3SEQ, ECO:0007744\|PDB:3SEZ, ECO:0007744\|PDB:3SYT, ECO:0007744\|PDB:3SZG

Chain	Residue	Details
A	ARG354
C	ASN471
C	GLY475
C	HIS501
D	ARG354
D	ASN471
D	GLY475
D	HIS501
A	ASN471
A	GLY475
A	HIS501
B	ARG354
B	ASN471
B	GLY475
B	HIS501
C	ARG354

site_id	SWS_FT_FI6
Number of Residues	4
Details	BINDING: BINDING => ECO:0000255\|HAMAP-Rule:MF_02090, ECO:0007744\|PDB:3SEQ, ECO:0007744\|PDB:3SEZ, ECO:0007744\|PDB:3SYT, ECO:0007744\|PDB:3SZG

Chain	Residue	Details
A	GLY366
B	GLY366
C	GLY366
D	GLY366

site_id	SWS_FT_FI7
Number of Residues	4
Details	BINDING: in other chain => ECO:0000255\|HAMAP-Rule:MF_02090, ECO:0007744\|PDB:3DLA, ECO:0007744\|PDB:3SEQ, ECO:0007744\|PDB:3SEZ, ECO:0007744\|PDB:3SZG

Chain	Residue	Details
A	ASN456
B	ASN456
C	ASN456
D	ASN456

site_id	SWS_FT_FI8
Number of Residues	4
Details	BINDING: BINDING => ECO:0000255\|HAMAP-Rule:MF_02090, ECO:0007744\|PDB:3SEQ, ECO:0007744\|PDB:3SYT, ECO:0007744\|PDB:3SZG

Chain	Residue	Details
A	THR480
B	THR480
C	THR480
D	THR480

site_id	SWS_FT_FI9
Number of Residues	4
Details	BINDING: in other chain => ECO:0000255\|HAMAP-Rule:MF_02090, ECO:0007744\|PDB:3SEQ, ECO:0007744\|PDB:3SEZ, ECO:0007744\|PDB:3SYT

Chain	Residue	Details
A	GLU485
B	GLU485
C	GLU485
D	GLU485

site_id	SWS_FT_FI10
Number of Residues	8
Details	BINDING: in other chain => ECO:0000255\|HAMAP-Rule:MF_02090, ECO:0007744\|PDB:3DLA, ECO:0007744\|PDB:3SEQ, ECO:0007744\|PDB:3SEZ, ECO:0007744\|PDB:3SYT, ECO:0007744\|PDB:3SZG

Chain	Residue	Details
A	TRP490
A	LYS635
B	TRP490
B	LYS635
C	TRP490
C	LYS635
D	TRP490
D	LYS635

site_id	SWS_FT_FI11
Number of Residues	4
Details	BINDING: in other chain => ECO:0007744\|PDB:3DLA, ECO:0007744\|PDB:3SZG

Chain	Residue	Details
A	SER661
B	SER661
C	SER661
D	SER661

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)